Component
Overoxidation of human MMUT-bound cob(II)alamin
Overoxidation of human MMUT-bound cob(II)alamin
1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.
How nutrients influence it
Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
How nutrients reach it in more than one step
Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.
Tracing routes…
What it does
Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.
What acts on it
ADP binding protected cob(II)alamin on human MMUT from air oxidation by stabilizing a solvent-shielded conformation.
Experimental context and source evidence
- cross_nutrient
- false
- evidence_location
- Full text Results; Figures 2-3, Table 3
- experimental_model
- Purified human proteins
- exposure
- ADP added to MMUT-bound cob(II)alamin under air
- limitations
- Structural/biochemical protection does not establish regulation by cellular energy charge.
- nutrient_topic
- Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. · Vitamin B12 (cobalamins)
- organism
- Homo sapiens
- plain_language
- ADP helped preserve an inactive B12 cofactor for repair in the human-protein assay.
- primary_references
- [gouda-2023-adp-repair] Bivalent molecular mimicry by ADP protects metal redox state and promotes coenzyme B12 repair. (2023). https://pubmed.ncbi.nlm.nih.gov/36888659/ DOI: 10.1073/pnas.2220677120
- tissue_or_cell_type
- Purified protein assay
Vitamin B12: mechanisms, deficiency and nutrient interactions (2026-09-17) · lines 1398–1410
AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified human proteins · source_derived_draft · unverified_draft
### adp-protects-mmut-cofactor-redox ADP binding protected cob(II)alamin on human MMUT from air oxidation by stabilizing a solvent-shielded conformation. Condition category: normal nutrient_topic: Vitamin B12 research collection; topical membership is not evidence of a direct dietary effect. plain_language: ADP helped preserve an inactive B12 cofactor for repair in the human-protein assay. organism: Homo sapiens tissue_or_cell_type: Purified protein assay experimental_model: Purified human proteins limitations: Structural/biochemical protection does not establish regulation by cellular energy charge. exposure: ADP added to MMUT-bound cob(II)alamin under air cross_nutrient: false evidence_location: Full text Results; Figures 2-3, Table 3 [gouda-2023-adp-repair] Bivalent molecular mimicry by ADP protects metal redox state and promotes coenzyme B12 repair. (2023). https://pubmed.ncbi.nlm.nih.gov/36888659/ DOI: 10.1073/pnas.2220677120
Complete structured claim and evidence
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.